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Does protease inhibitor inhibit complement activation caused by the immune complex associated with islet cell surface
The Journal of International Medical Research
|May 1, 1991
Summary
Nafamostat mesylate effectively inhibits complement activation in sera from children with insulin-dependent diabetes mellitus. This protease inhibitor blocks both classical and alternative complement pathways linked to islet cell surface antibodies.
Area of Science:
- Immunology
- Endocrinology
- Pharmacology
Background:
- Insulin-dependent diabetes mellitus (IDDM) is an autoimmune disease targeting pancreatic beta cells.
- Islet cell surface antibodies (ICSA) are key biomarkers in early IDDM.
- Complement system activation plays a role in antibody-mediated islet cell destruction.
Purpose of the Study:
- To investigate the effect of nafamostat mesylate, a protease inhibitor, on complement-dependent cytotoxicity mediated by ICSA.
- To determine if nafamostat mesylate can inhibit both classical and alternative complement pathways in the context of IDDM sera.
Main Methods:
- Sera from seven children with recent-onset IDDM were used.
- 51Cr-labeled rat islet cells were incubated with ICSA and human AB serum.
- Complement-dependent cytotoxicity was measured after treatment with nafamostat mesylate, EGTA, or EDTA.
Main Results:
- Nafamostat mesylate significantly inhibited ICSA-mediated cytotoxicity (2.8 +/- 1.8%).
- Inhibition by nafamostat mesylate was comparable to EDTA and significantly greater than EGTA.
- The protease inhibitor blocked complement activation via both classical and alternative pathways.
Conclusions:
- Nafamostat mesylate effectively inhibits complement activation triggered by ICSA.
- This suggests a potential therapeutic role for protease inhibitors in managing autoimmune diabetes by preventing beta cell destruction.